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pubmed-article:9564602pubmed:abstractTextMAO-A and -B are defined by their substrate and inhibitor preferences. To determine which regions of the isoenzymes confer these preferences, we have constructed six chimeric MAO enzymes by reciprocally exchanging corresponding N-terminal, C-terminal, and internal segments of MAO-A and -B then determined the catalytic properties of these chimeric enzymes. N-terminal chimerics A45B and B36A were made by exchanging amino acid segments 1-45 and 1-36 of MAO-A and -B respectively. C-terminal chimerics A402B and B393A were made by exchanging amino acid segments 403-527 and 394-520 of MAO-A and -B respectively, and internal chimerics AB161-375A and BA152-366B were made by exchanging amino acid segments 161-375 and 152-366 of MAO-A and -B respectively. The enzymatic properties observed for the chimerics suggest that the exchanged internal regions but not the N- or C-terminal regions confer substrate and inhibitor preferences.lld:pubmed
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pubmed-article:9564602pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:9564602pubmed:year1998lld:pubmed
pubmed-article:9564602pubmed:articleTitleDetermination of regions important for monoamine oxidase (MAO) A and B substrate and inhibitor selectivities.lld:pubmed
pubmed-article:9564602pubmed:affiliationDepartment of Molecular Pharmacology and Toxicology, School of Pharmacy, University of Southern California, Los Angeles, USA.lld:pubmed
pubmed-article:9564602pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9564602pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:9564602pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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